SSN2_YEAST
ID SSN2_YEAST Reviewed; 1420 AA.
AC P38931; D6VT69;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 13;
DE AltName: Full=Mediator complex subunit 13;
DE AltName: Full=Protein SCA1;
DE AltName: Full=Suppressor of RNA polymerase B SSN2;
GN Name=SSN2; Synonyms=MED13, NUT8, RYE3, SCA1, SRB9, UME2;
GN OrderedLocusNames=YDR443C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7774808; DOI=10.1101/gad.9.8.897;
RA Hengartner C.J., Thompson C.M., Zhang J., Chao D.M., Liao S.-M.,
RA Koleske A.J., Okamura S., Young R.A.;
RT "Association of an activator with an RNA polymerase II holoenzyme.";
RL Genes Dev. 9:897-910(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8725217; DOI=10.1093/genetics/143.2.661;
RA Yuryev A., Corden J.L.;
RT "Suppression analysis reveals a functional difference between the serines
RT in positions two and five in the consensus sequence of the C-terminal
RT domain of yeast RNA polymerase II.";
RL Genetics 143:661-671(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP IDENTIFICATION IN THE SRB8-11 COMPLEX, AND FUNCTION OF THE SRB8-11 COMPLEX.
RX PubMed=12200444; DOI=10.1074/jbc.m207195200;
RA Borggrefe T., Davis R., Erdjument-Bromage H., Tempst P., Kornberg R.D.;
RT "A complex of the Srb8, -9, -10, and -11 transcriptional regulatory
RT proteins from yeast.";
RL J. Biol. Chem. 277:44202-44207(2002).
RN [6]
RP FUNCTION, PHOSPHORYLATION AT SER-608 BY PKA, AND MUTAGENESIS OF SER-608 AND
RP SER-1236.
RX PubMed=15225552; DOI=10.1016/j.molcel.2004.05.021;
RA Chang Y.-W., Howard S.C., Herman P.K.;
RT "The Ras/PKA signaling pathway directly targets the Srb9 protein, a
RT component of the general RNA polymerase II transcription apparatus.";
RL Mol. Cell 15:107-116(2004).
RN [7]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [8]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [9]
RP FUNCTION.
RX PubMed=16109375; DOI=10.1016/j.molcel.2005.06.033;
RA van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,
RA van Leenen D., Holstege F.C.P.;
RT "Mediator expression profiling epistasis reveals a signal transduction
RT pathway with antagonistic submodules and highly specific downstream
RT targets.";
RL Mol. Cell 19:511-522(2005).
RN [10]
RP FUNCTION OF THE SRB8-11 COMPLEX.
RX PubMed=15601835; DOI=10.1128/mcb.25.1.114-123.2005;
RA Larschan E., Winston F.;
RT "The Saccharomyces cerevisiae Srb8-Srb11 complex functions with the SAGA
RT complex during Gal4-activated transcription.";
RL Mol. Cell. Biol. 25:114-123(2005).
RN [11]
RP FUNCTION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-375, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; SER-425; SER-636 AND
RP SER-748, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375; THR-601 AND SER-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC RNA polymerase II RPB1 at serines 2 and 5.
CC {ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:15225552,
CC ECO:0000269|PubMed:15601835, ECO:0000269|PubMed:16076843,
CC ECO:0000269|PubMed:16109375, ECO:0000269|PubMed:16630888}.
CC -!- SUBUNIT: Component of the SRB8-11 complex which consists of SRB8,
CC SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates
CC with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin
CC pair also associate with the RNA polymerase II holoenzyme.
CC {ECO:0000269|PubMed:12200444}.
CC -!- INTERACTION:
CC P38931; P07273: DST1; NbExp=2; IntAct=EBI-18059, EBI-19168;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Phosphorylated. PKA-dependent phosphorylation at 'Ser-608' is
CC enhanced by activation of the RAS signaling pathway.
CC {ECO:0000269|PubMed:15225552}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 13 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23812; AAA91316.1; -; Genomic_DNA.
DR EMBL; U09176; AAA18614.1; -; Unassigned_DNA.
DR EMBL; U33007; AAB64875.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12279.1; -; Genomic_DNA.
DR PIR; B57062; B57062.
DR RefSeq; NP_010731.3; NM_001180751.3.
DR PDB; 7KPV; EM; 3.80 A; D=1-1420.
DR PDB; 7KPX; EM; 4.40 A; D=1-1420.
DR PDBsum; 7KPV; -.
DR PDBsum; 7KPX; -.
DR AlphaFoldDB; P38931; -.
DR SMR; P38931; -.
DR BioGRID; 32498; 305.
DR ComplexPortal; CPX-1853; CKM complex.
DR DIP; DIP-5947N; -.
DR IntAct; P38931; 16.
DR MINT; P38931; -.
DR STRING; 4932.YDR443C; -.
DR iPTMnet; P38931; -.
DR MaxQB; P38931; -.
DR PaxDb; P38931; -.
DR PRIDE; P38931; -.
DR EnsemblFungi; YDR443C_mRNA; YDR443C; YDR443C.
DR GeneID; 852053; -.
DR KEGG; sce:YDR443C; -.
DR SGD; S000002851; SSN2.
DR VEuPathDB; FungiDB:YDR443C; -.
DR eggNOG; KOG3600; Eukaryota.
DR GeneTree; ENSGT00390000007801; -.
DR HOGENOM; CLU_242296_0_0_1; -.
DR InParanoid; P38931; -.
DR OMA; FSRELWC; -.
DR BioCyc; YEAST:G3O-29975-MON; -.
DR PRO; PR:P38931; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P38931; protein.
DR GO; GO:1990508; C:CKM complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0000435; P:positive regulation of transcription from RNA polymerase II promoter by galactose; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR009401; Med13_C.
DR InterPro; IPR021643; Mediator_Med13_N.
DR Pfam; PF06333; Med13_C; 1.
DR Pfam; PF11597; Med13_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1420
FT /note="Mediator of RNA polymerase II transcription subunit
FT 13"
FT /id="PRO_0000072215"
FT REGION 416..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 608
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:15225552,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 608
FT /note="S->A: Loss of function; when associated with A-
FT 1236."
FT /evidence="ECO:0000269|PubMed:15225552"
FT MUTAGEN 1236
FT /note="S->A: Loss of function; when associated with A-608."
FT /evidence="ECO:0000269|PubMed:15225552"
FT CONFLICT 38
FT /note="D -> E (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="E -> V (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="T -> S (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
FT CONFLICT 877..878
FT /note="VK -> GE (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="T -> P (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
FT CONFLICT 1284
FT /note="Y -> S (in Ref. 2; AAA18614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1420 AA; 160001 MW; 7F6CF4BBE0FAC918 CRC64;
MSSDASTYRL EDVLSSFYRV EKIKKINYHQ YISKAQNDQW SIQMEFMLRK QDPKTLVALL
SRDLWCFSIN DDPVPTPPAI EHKPVSPDKI GTFTADYSKP NLPPHYALFL KALRRKIYIN
LALGSHNKLI QFGNACISLS GVPNYLVQLE PHLFVNGDLT VSLCAKNMGL VPMKEENLEE
SFLSKHALYL APSGIRMHLA PASKQGYLIT PPKHTELLLT TLSVSHGINL QNKKNLKWVA
VVPDLGHLNG HTPTIASYLT PLLEAKKLVW PLHLIFAQPV ADIENSTSGD PSEFHCLQDA
LDAIDDFIQL KQTAAYRTPG SSGVLSSNIA GTNPLSSDGA YTEQFQHYKN NSISSQPASY
HSVQETNKIS PKDFSPNFTG IDKLMLSPSD QFAPAFLNTP NNNINENELF NDRKQTTVSN
DLENSPLKTE LEANGRSLEK VNNSVSKTGS VDTLHNKEGT LEQREQNENL PSDKSDSMVD
KELFGEDEDE DLFGDSNKSN STNESNKSIS DEITEDMFEM SDEEENNNNK SINKNNKEMH
TDLGKDIPFF PSSEKPNIRT MSGTTKRLNG KRKYLDIPID EMTLPTSPLY MDPGAPLPVE
TPRDRRKSVF APLNFNPIIE NNVDNKYKSG GKFSFSPLQK EEALNFDISM ADLSSSEEEE
DEEENGSSDE DLKSLNVRDD MKPSDNISTN TNIHEPQYIN YSSIPSLQDS IIKQENFNSV
NDANITSNKE GFNSIWKIPQ NDIPQTESPL KTVDSSIQPI ESNIKMTLED NNVTSNPSEF
TPNMVNSEIS NLPKDKSGIP EFTPADPNLS FESSSSLPFL LRHMPLASIP DIFITPTPVV
TISEKEQDIL DLIAEQVVTD YNILGNLGIP KIAYRGVKDC QEGLITTTML QLFSTFDRLN
GNDTISKFYN MKQPYVFVKK HHELIKVKHD SQPFIKFLNF RPPNGIKNFK SLLLSSSFKE
DCLSFAPTLS QTYINQELGF CELLKLTNED PPGLMYLKAF DKNKLLLLAA QIVSYCSNNK
NSIKNVPPIL IILPLDNATL TELVDKANIF QVIKNEVCAK MPNIELYLKV IPMDFIRNVL
VTVDQYVNVA ISIYNMLPPK SVKFTHIAHT LPEKVNFRTM QQQQMQQQQQ QQQQQQNNST
GSSSIIYYDS YIHLAYSRSV DKEWVFAALS DSYGQGSMTK TWYVGNSRGK FDDACNQIWN
IALNLASKKF GKICLILTRL NGILPDDELM NWRRLSGRNI HLAVVCVDDN SKISFIDEDK
LYPSFKPIYK DTRFGGRMDM TRLYDYEIRD IDQDIHGIVF QHPFPLAHSQ HRCAIRSGAL
IKFKKCDGDT VWDKFAVNLL NCPHSDSTQL LETILEEFRN LAALNVWYGL SDGEDGHIPW
HILAVKKMMN TLVHTRVKIA NTSAATVHTA TSSSIILSDK
